Q9EQU3: Toll-like receptor 9 (Tlr9)

Toll-like receptor 9 (Tlr9) is a 1032-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9EQU3.

Gene
Tlr9
Organism
Mus musculus
Length
1032 residues
Mean pLDDT
87.8
Model
AF-Q9EQU3-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate68%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Key component of innate and adaptive immunity (PubMed:31408613). TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms (PubMed:31408613). TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides (PubMed:31408613). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:14993594, PubMed:17474149, PubMed:18820679, PubMed:18931679, PubMed:21402738, PubMed:25686612). Also acts via ADCY7, leading to cyclic di-AMP (c-di-AMP) synthesis and activation of the NLRP3 inflammasome…

Subunit structure

Monomer and homodimer. Exists as a monomer in the absence of unmethylated cytidine-phosphate-guanosine (CpG) ligand. Proteolytic processing of an insertion loop (Z-loop) is required for homodimerization upon binding to the unmethylated CpG ligand leading to its activation (By similarity). Interacts with MYD88 via their respective TIR domains (PubMed:18820679). Interacts with BTK (By similarity).…

Subcellular location

Endoplasmic reticulum membrane, Endosome, Lysosome, Cytoplasmic vesicle, phagosome

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3WPFX-ray1.96 ÅA=26-818
3WPGX-ray2.25 ÅA=26-818
3WPIX-ray2.25 ÅA=26-818
5ZLNX-ray2.3 ÅA/B=26-818
3WPHX-ray2.33 ÅA=26-818
4QDHX-ray2.4 ÅA/B=478-753

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